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조회 434  인쇄하기 주소복사 트위터 공유 페이스북 공유 
Unique Unfoldase/Aggregase Activity of a Molecular Chaperone Hsp33 in its Holding-Inactive State
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The various chaperone activities of heat shock proteins contribute to ensuring cellular proteostasis. Here, we demonstrate the non-canonical unfoldase activity as an inherent functionality of the prokaryotic molecular chaperone, Hsp33. Hsp33 was originally identified as a holding chaperone that is post-translationally activated by oxidation. However, in this study, we verified that the holding-inactive reduced form of Hsp33 (RHsp33) strongly bound to the translational elongation factor, EF-Tu. This interaction was critically mediated by the redox-switch domain of RHsp33 and the guanine nucleotide-binding domain of EF-Tu. The bound RHsp33, without undergoing any conformational change, catalyzed the EF-Tu aggregation by evoking the aberrant folding of EF-Tu to expose hydrophobic surfaces. Consequently, the oligomers/aggregates of EF-Tu, but not its functional monomeric form, were highly susceptible to proteolytic degradation by Lon protease. These findings present a unique example of an ATP-independent molecular chaperone with distinctive dual functions—as an unfoldase/aggregase and as a holding chaperone—depending on the redox status. It is also suggested that the unusual unfoldase/aggregase activity of RHsp33 can contribute to cellular proteostasis by dysregulating EF-Tu under heat-stressed conditions.

ANS, 8-anilino-1-naphthalene sulfonic acid; CD, circular dichroism; D2, domain-II; D3, domain-III; DTT, dithiothreitol; EDTA, ethylenediaminetetraacetic acid; EF-Ts, elongation factor thermal-stable; EF-Tu, elongation factor thermal-unstable; GD, guanidine nucleotide-binding domain; Hsp33, heat shock protein 33; ITC, isothermal titration calorimetry; MLD, middle linker domain; RSD, redox-switch domain; TROSY, transverse relaxation optimized spectroscopy

Keywords : proteostasis; protein quality control; protein turnover; protein misfolding; protein aggregation

논문정보 F1000선정
- 형식: Research article
- 게재일: 2019년 03월 (BRIC 등록일 2019-09-20)
- 연구진: 국내연구진태극기
- 분야: Biochemistry, Molecular_Biology
- 추천: Faculty of 1000 Biology
- 추천사유: Collet J and Goemans C: F1000Prime Recommendation of [Jo KS et al., J Mol Biol 2019 431(7):1468-1480]. In F1000Prime, 18 Sep 2019; 10.3410/f.735222321.793565263
  댓글 1
회원작성글 김진23  (2019-10-02 04:26)
내일 회사 가서 자랑 해도 될까요? ㅎㅎ
진심으로 축하드립니다~!!
원형식 님 전체논문보기 >
석승현 (서울대학교)
이봉진 (서울대학교)
임후강 (서울대학교)
조규성 (건국대학교)
관련분야 논문보기


Google (by Hyung-Sik Won)
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프리미엄 Bio일정 Bio일정 프리미엄 안내
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사전접수: ~2019.11.23
날짜: 2019.11.28
장소: 호텔프리마(강남구)
2020년도 신약개발지원센터 기반기술구축사업 ‘최적화 기술지원’ 분야 신규과제 공고
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